The TagB Protein in Bacillus subtilis 168 Is an Intracellular Peripheral Membrane Protein That Can Incorporate Glycerol Phosphate onto a Membrane-bound Acceptor in Vitro

Genes involved in the synthesis of poly(glycerol phosphate) wall teichoic acid have been identified in the tag locus of the model Gram-positive organism Bacillus subtilis 168. The functions of most of these gene products are predictable from sequence similarity to characterized proteins and have provided limited insight into the intracellular synthesis and translocation of wall teichoic acid. Nevertheless, critical steps of poly(glycerol phosphate) teichoic acid polymerization continue to be a puzzle. TagB and TagF, encoded in the tag locus, do not show sequence similarity to characterized proteins. We recently showed that recombinant TagF could catalyze glycerol phosphate polymerization in vitro. Based largely on homology to TagF, the TagB protein has been proposed to catalyze either an intracellular glycerophosphotransfer reaction or the extracellular teichoic acid/peptidoglycan ligation reaction. Here we have taken steps to characterize TagB, particularly through in vivo localization studies and in vitro biochemical assay, in order to make a case for either role in teichoic acid biogenesis. We have shown that TagB associates peripherally with the intracellular face of the cell membrane in vivo. We have also produced recombinant TagB and used it to demonstrate the enzymatic incorporation of labeled glycerol phosphate onto a membrane-bound acceptor. The data collected from this and the accompanying study (Schertzer, J. W., Bhavsar, A. P., and Brown, E. D. (2005) J. Biol. Chem. 280, 36683–36690) are strongly supportive of a role for TagB in B. subtilis 168 teichoic acid biogenesis as the CDP-glycerol:N-acetyl-β-d-mannosaminyl-1,4-N-acetyl-d-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase. Here we use the trivial name “Tag primase.” Genes involved in the synthesis of poly(glycerol phosphate) wall teichoic acid have been identified in the tag locus of the model Gram-positive organism Bacillus subtilis 168. The functions of most of these gene products are predictable from sequence similarity to characterized proteins and have provided limited insight into the intracellular synthesis and translocation of wall teichoic acid. Nevertheless, critical steps of poly(glycerol phosphate) teichoic acid polymerization continue to be a puzzle. TagB and TagF, encoded in the tag locus, do not show sequence similarity to characterized proteins. We recently showed that recombinant TagF could catalyze glycerol phosphate polymerization in vitro. Based largely on homology to TagF, the TagB protein has been proposed to catalyze either an intracellular glycerophosphotransfer reaction or the extracellular teichoic acid/peptidoglycan ligation reaction. Here we have taken steps to characterize TagB, particularly through in vivo localization studies and in vitro biochemical assay, in order to make a case for either role in teichoic acid biogenesis. We have shown that TagB associates peripherally with the intracellular face of the cell membrane in vivo. We have also produced recombinant TagB and used it to demonstrate the enzymatic incorporation of labeled glycerol phosphate onto a membrane-bound acceptor. The data collected from this and the accompanying study (Schertzer, J. W., Bhavsar, A. P., and Brown, E. D. (2005) J. Biol. Chem. 280, 36683–36690) are strongly supportive of a role for TagB in B. subtilis 168 teichoic acid biogenesis as the CDP-glycerol:N-acetyl-β-d-mannosaminyl-1,4-N-acetyl-d-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase. Here we use the trivial name “Tag primase.” The major class of anionic polymer in Gram-positive bacteria is teichoic acid. Growing evidence suggests that these phosphate-rich polyol polymers are essential to the viability of the model Gram-positive, Bacillus subtilis (1Bhavsar A.P. Beveridge T.J. Brown E.D. J. Bacteriol. 2001; 183: 6688-6693Crossref PubMed Scopus (51) Google Scholar, 2Boylan R.J. Mendelson N.H. J. Bacteriol. 1969; 100: 1316-1321Crossref PubMed Google Scholar, 3Boylan R.J. Mendelson N.H. Brooks D. Young F.E. J. Bacteriol. 1972; 110: 281-290Crossref PubMed Google Scholar, 4Mauel C. Young M. Margot P. Karamata D. Mol. Gen. Genet. 1989; 215: 388-394Crossref PubMed Scopus (59) Google Scholar, 5Briehl M. Pooley H.M. Karamata D. J. Gen. Microbiol. 1989; 135: 1325-1334Google Scholar). The bulk of the genes for teichoic acid biosynthesis in B. subtilis 168 are indispensable and situated in the tag operons, tagAB, tagDEF, and tagGH, which code for the synthesis of a poly(glycerol phosphate) polymer (6Lazarevic V. Karamata D. Mol. Microbiol. 1995; 16: 345-355Crossref PubMed Scopus (115) Google Scholar, 7Mauel C. Young M. Karamata D. J. Gen. Microbiol. 1991; 137: 929-941Crossref PubMed Scopus (73) Google Scholar). Indeed, we recently verified that the tagB and tagF gene products were essential to the viability of B. subtilis 168 (8Bhavsar A.P. Erdman L.K. Schertzer J.W. Brown E.D. J. Bacteriol. 2004; 186: 7865-7873Crossref PubMed Scopus (83) Google Scholar). Functional predictions have been made for most of the gene products on the basis of homology to characterized enzymes. It is noteworthy that biochemical characterization of these functions has been restricted so far to TagD, the CDP-glycerol pyrophosphorylase (9Park Y.S. Sweitzer T.D. Dixon J.E. Kent C. J. Biol. Chem. 1993; 268: 16648-16654Abstract Full Text PDF PubMed Google Scholar, 10Badurina D.S. Zolli-Juran M. Brown E.D. Biochim. Biophys. Acta. 2003; 1646: 196-206Crossref PubMed Scopus (35) Google Scholar), TagF, the teichoic acid glycerol phosphate (Tag) 3The abbreviations used are:Tagteichoic acid glycerol phosphateGFPgreen fluorescent proteinPBSphosphate-buffered salineCHAPS3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonateHPLChigh performance liquid chromatography. polymerase (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar), and MnaA, the N-acetylglucosamine 2-epimerase (12Soldo B. Lazarevic V. Pooley H.M. Karamata D. J. Bacteriol. 2002; 184: 4316-4320Crossref PubMed Scopus (34) Google Scholar). A model for teichoic acid biogenesis has been proposed based largely on the functional predictions for the tag genes (13Lazarevic V. Abellan F.X. Moller S.B. Karamata D. Mauel C. Microbiology. 2002; 148: 815-824Crossref PubMed Scopus (69) Google Scholar). Significant gaps remain, however, in our understanding of teichoic acid biogenesis. Most notably, the step immediately preceding glycerol phosphate polymerization, the transfer of glycerol phosphate to an undecaprenyl-pyrophosphoryl-N-acetylglucosaminyl-N-acetylmannosamine acceptor, and also the final step in teichoic acid biogenesis, the ligation of teichoic acid to peptidoglycan (14Pooley H.M. Karamata D. Ghuysen J.M. Hakenbeck R. Bacterial Cell Wall. Elsevier, Amsterdam1994: 187-198Google Scholar), remain essentially uncharacterized. teichoic acid glycerol phosphate green fluorescent protein phosphate-buffered saline 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate high performance liquid chromatography. We are particularly interested in identifying the unknown enzymes catalyzing the glycerophosphotransfer and ligation reactions outlined above. The reactions are chemically similar a reaction the is a the of or the of and the has a CDP-glycerol or that Indeed, the enzymes catalyzing reactions be to similarity and homology with the glycerol phosphate TagF homology to characterized enzymes homology and to the TagB protein C. Young M. Karamata D. J. Gen. Microbiol. 1991; 137: 929-941Crossref PubMed Scopus (73) Google Scholar). is the of TagF, a to as a glycerol phosphate so sequence similarity to TagB not immediately an functional for Nevertheless, the that TagB either the glycerophosphotransfer to the or the polymer ligation to acid is a based on homology to TagF, as H.M. Abellan F.X. Karamata D. J. Bacteriol. PubMed Google Scholar). The on TagB is also of a B. subtilis and to a in that the of CDP-glycerol the H.M. Abellan F.X. Karamata D. J. Gen. Microbiol. 1991; 137: PubMed Scopus Google Scholar). be with a role for TagB as a that of the glycerol phosphate It also however, that the to which teichoic acid as a H.M. Abellan F.X. Karamata D. J. Gen. Microbiol. 1991; 137: PubMed Scopus Google Scholar). that teichoic acid and to the extracellular face of the membrane and be with a teichoic acid/peptidoglycan for based on sequence of TagB A. B. J. Mol. Biol. 2001; PubMed Scopus Google and Biol. Chem. 1993; the of a situated and predictions that TagB is a membrane the bulk of the protein is of is the Karamata and C. Young M. Karamata D. J. Gen. Microbiol. 1991; 137: 929-941Crossref PubMed Scopus (73) Google of a which the identified and J. PubMed Scopus Google Scholar). in B. subtilis in localization of proteins to the extracellular face of the the predictions from sequence are most with a role for TagB as the teichoic acid/peptidoglycan this we have the in vivo and in vitro of TagB to biochemical role in teichoic acid characterize the localization of TagB we have a of recombinant TagB and produced TagB We have provided evidence for membrane localization and have characterized this to show that it is and and a of TagB to the green fluorescent protein we have provided the in vivo of a teichoic acid which showed localization of TagB to the cell and we have that TagB is of catalyzing the incorporation of glycerol phosphate from CDP-glycerol to a membrane-bound in vitro. a role for TagB as the CDP-glycerol:N-acetyl-β-d-mannosaminyl-1,4-N-acetyl-d-glucosaminyldiphosphoundecaprenyl glycerophosphotransferase. Here we to this as the “Tag to and functional with the Bacterial and used in this study are in were from for and B. subtilis were as outlined J. A and and P. P. for and for D. Scholar), for were from the used a of and as and and used in this subtilis M. Pooley H.M. Karamata D. J. Gen. Microbiol. 1989; 135: 1325-1334Google with with with J. Mol. Biol. PubMed Scopus Google of A. PubMed Scopus Google from in with tagB from B. J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google of tagB in with tagB tag with tag for B. R. PubMed Scopus Google with tagB with with tagB tag with J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google with tagB in a of in the TagB, the tagB and The into and of the to an into the to the of TagB were protein of TagB or the and were from J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google and J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google with J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google and The products were into the of and and that the of the to the of the were verified of the in vivo TagB localization the from into R. PubMed Scopus Google Scholar), and to The tagB from to of to TagB, the from of A. PubMed Scopus Google into to tagB with and which a the in the sequence of and into and in the The has the and the TagB and The and used to tagB in were into B. subtilis 168 through E. J. Mol. Biol. PubMed Scopus Google Scholar). were for and verified of from the of TagB and into for protein were in with with and with an of were with for were and The cell in and through a for and the in a for The in of A and to for on with for in a The with and to to onto a with of a from to protein into and to the for protein into phosphate-buffered saline glycerol and for in of to the to We of the on to the TagB proteins. were with and protein were in with for with and with were an with The similar to that outlined for that the used for proteins from the were on an were were the of as a protein PubMed Scopus Google Scholar). and B. subtilis were were from a that and to an to the of a The in a to to the B. subtilis cell to the of R. J. Bacteriol. 1995; PubMed Google Scholar). were to and were on a with a and with with the and and were a of TagB in B. and were in of with with an of were and Cell were in Bacillus and to the were through a and the in a for to The in a for and the in an for from this step and the in an of membrane and the membrane were either or transfer to a either or to used as were the to the of B. subtilis from were in a for and the in membrane of membrane to of and were as A. 2003; PubMed Scopus Google Scholar), that used for were onto a the were in a for The were into and The and were with an The acid and were in the of membrane and were transfer to a as outlined above. of TagB in B. were from essentially the of and R. D. J. Bacteriol. PubMed Google Scholar), that the from as membrane through a cell as outlined were in a for and the in an of and were with either or The final of in reactions to the of the were for and the of to were in a for and the for The in and in an of were in a for and the for The with steps in a the in an of and were transfer to a as outlined above. of with the of reaction of and of The reaction and The reaction for and through an to The reaction to CDP-glycerol to J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google for essentially to Schertzer and Brown (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar), that B. subtilis were for to use in the to the the of B. subtilis 168 membrane and CDP-glycerol in for and with to were of TagB reactions were as and the final were in for and for acid were to and Microbiology. 2002; 148: PubMed Scopus Google Scholar), and acid to J. PubMed Scopus Google for were to of TagB TagB reaction to of B. subtilis 168 membrane and CDP-glycerol of and for A reaction also the were with were to acid as outlined above. The and through an A of the to and for to the TagB reaction to glycerol phosphate (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar, J. J. 1972; PubMed Scopus (73) Google Scholar). were and high performance liquid a with of the of recombinant TagB from E. TagB in the membrane of E. and we that of could be from the membrane in the of a could be to a step not the of TagB, we of the protein and that it to a not We also the protein to and a of not in with the of of the We used this protein as to an The protein also used to the TagB to the in B. of TagB in the tagB gene into a that from the R. PubMed Scopus Google Scholar). from and were for of of TagB in from verified of protein also our to of TagB in B. to a of this a that has been of the and of the tagB gene C. Young M. Karamata D. J. Gen. Microbiol. 1991; 137: 929-941Crossref PubMed Scopus (73) Google Scholar). the localization of TagB in from of the showed that TagB to the membrane of B. subtilis of TagD, a glycerol phosphate involved in teichoic acid biosynthesis (9Park Y.S. Sweitzer T.D. Dixon J.E. Kent C. J. Biol. Chem. 1993; 268: 16648-16654Abstract Full Text PDF PubMed Google Scholar), and a membrane protein involved in cell A. PubMed Scopus Google Scholar), used to the of the and membrane with of membrane in the The suggests that TagB be TagB with the A. B. J. Mol. Biol. 2001; PubMed Scopus Google and Biol. Chem. 1993; the of a and of of this sequence an to the and membrane of TagB, the membrane from with or were through a to of protein from the membrane to the with either or showed of TagB from the membrane that TagB is peripherally with the cell an predictions of TagB with the of the a of the of TagB with the membrane to TagB with the or extracellular face of the cell and membrane from were used in a were to and of the of TagB protein in the and to be of similar to protein and A of a TagB in the We that this a that from the of TagB in the of the the the TagB were with to with to the a of TagB not membrane were with in the of and We an in the of TagB in the this of TagB not in the of the the data from the membrane that of the studies and that TagB is to the face of the cell has also been the of C. J. Bacteriol. PubMed Google Scholar), to the E. and genes were made to tagB the the and not in of TagB in a made to the green fluorescent protein the of of we to the cell of B. subtilis of showed in a were in data that TagB is to the face of the membrane in B. with the biochemical Indeed, of in and membrane of showed essentially the in the membrane as that with not we that the not on the localization of we that the in the of an as in A and The protein also for to a B. subtilis the that a in tagB R.J. Mendelson N.H. J. Bacteriol. 1969; 100: 1316-1321Crossref PubMed Google Scholar, 7Mauel C. Young M. Karamata D. J. Gen. Microbiol. 1991; 137: 929-941Crossref PubMed Scopus (73) Google Scholar). We that the to the the in a similar to TagB not that the protein functional in vivo that the localization of the protein of onto a B. subtilis and Brown (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google on an that the incorporation of labeled glycerol from onto an in B. subtilis in the polymerization of glycerol phosphate We that the the of a glycerol phosphate onto the in B. subtilis we were that the from a be that for the is the of in the membrane the the be the to the that the of glycerol phosphate for the we the to a CDP-glycerol phosphate not so we a enzymatic synthesis for the of the enzymatic glycerol with a step that to based not The labeled glycerol phosphate to CDP-glycerol and this reaction to not the membrane localization of TagB in vivo and the for a membrane sequence the of TagB, we were that our a we a recombinant TagB that a the of the sequence the We that of this protein the and in the membrane incorporation assay, we were to incorporation of into the membrane of B. subtilis 168 and shown in this for with and also with from B. subtilis not A of for from this the for this we to the of membrane B. subtilis to the reaction. that the reaction showed a on membrane and to the an of for the membrane the were with B. subtilis 168 it that the of membrane not in the and this the of this is in with the of B. subtilis P. and E. D. Brown, of in that TagB the of glycerol phosphate to the of the of the to the of the the TagB reaction be into an the of the TagB reaction it to acid J. J. 1972; PubMed Scopus (73) Google Scholar). We in vitro and the membrane that to with either acid or The are shown in and demonstrate that of the onto the membrane could be either a the of the labeled CDP-glycerol also and to be characterization of TagB reaction for reaction in reaction in in for in in in a We characterized the reaction of the acid chromatography. shown in the reaction in The of the on and with a data not The and with a glycerol phosphate data not acid of the acid in the of the bulk of the reactions showed in the of TagB to that the we in the membrane incorporation to and not to a we to the the accompanying J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar), we showed that in TagB and TagF were for to a in in vivo. the TagF in vitro J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). We to these to TagB and a of to in the in vitro and enzymes were and the are shown in showed to the A of and to similar of TagB protein in the TagB were similar the it that the of protein in the We that the to a in the a from the we a in with this our that the glycerophosphotransfer is to The synthesis of polyol phosphate polymers to wall teichoic acid in Gram-positive largely biochemical the critical steps of polymerization, and of poly(glycerol phosphate) teichoic acid to the acid of peptidoglycan continue to be a puzzle. Based largely on homology to TagF, the it has been that the TagB protein catalyze either the or these functions are to be intracellular and the we have provided the evidence for membrane of this protein and have shown that TagB associates peripherally with the face of the cell with data the enzymatic incorporation of glycerol phosphate from CDP-glycerol to a membrane-bound that is to recombinant TagB, the biochemical characterization of TagB and TagB as the in B. subtilis 168. in vivo studies of TagB that to a understanding of role in teichoic acid biogenesis. and in vivo of TagB were with membrane of this teichoic acid is not acid biosynthesis on an in the cell as the of teichoic acid is to in to the cell the in the is to the membrane B. Lazarevic V. Karamata D. Microbiology. 2002; 148: PubMed Scopus Google Scholar). the TagF, has been shown to with from B. subtilis (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar, H.M. Abellan F.X. Karamata D. J. Bacteriol. PubMed Google Scholar). The to this is the synthesis of used in the of teichoic acid. of the of TagB with B. subtilis a in to predictions the of an situated and of TagB that be for of the protein through the membrane we have that TagB is not an membrane we were interested to that of this sequence a A similar has been identified the of the and involved in cell and shown to be for the of these proteins with the membrane in E. J. Mol. Microbiol. PubMed Scopus Google Scholar, A. 2002; PubMed Scopus Google Scholar, J. Mol. Microbiol. 2003; 345-355Crossref PubMed Scopus Google Scholar). the the in TagB not an for an It be that the face of the TagB with an protein situated on the into the and for a membrane-bound protein are it be that of high TagB with the that membrane not be that membrane is of a membrane-bound We have also and that TagB is the cell and with the face of the cell TagB an for are to be restricted to the extracellular face of the cell membrane in Gram-positive bacteria J. Bacteriol. 1995; PubMed Scopus Google Scholar, J. Bacteriol. Google Scholar). suggests that the sequence and of TagB is not a the of our a study of the protein in B. and R. M. J.M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar), to We have the membrane localization of TagB in vivo of a of TagB to the green fluorescent the in vivo localization of a protein involved in teichoic acid synthesis and the the the teichoic acid and involved in cell wall biosynthesis in B. we not localization into as or that TagB not with the identified proteins and that have been shown to peptidoglycan incorporation R. J. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, J. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). It be however, that our fluorescent with to protein and this have our to localization Nevertheless, we were interested to a for protein could not be the indispensable of teichoic acid this to the that be a role for enzymes in cell C. A. C. Karamata D. Microbiology. 1995; PubMed Scopus Google has that enzymes are involved in biogenesis, to a in the teichoic acid and cell it is the of to TagB protein in the of to this the to the biochemical of TagB homology to the TagF protein and of the proteins are of a of identified sequence similarity to proteins of J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). the that recombinant TagF could catalyze poly(glycerol phosphate) polymerization in vitro (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar), it based on homology to TagF, the TagB protein a to catalyze the or peptidoglycan of which are chemically to that the The that TagB could catalyze the incorporation of phosphate from to a membrane-bound is the biochemical for TagB to our the of to the as the of incorporation with and the of TagB is that for TagF it is to that the reaction on CDP-glycerol not in this and we be that the of this Indeed, to the incorporation of a of labeled glycerol phosphate in the TagB in vitro assay, the of CDP-glycerol the of CDP-glycerol in the TagF polymerase to be (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar). the TagB in this study be a of the of the to use in the in vitro We the that the of glycerol phosphate incorporation that TagB the on membrane of TagB and TagF were similar of that the reactions be in vivo as in of teichoic acid of the in vitro TagB reaction that it from the membrane acid and are with the proposed of the reaction that it and It to that these also be in the membrane-bound acceptor. the of glycerol phosphate to the the of the J. PubMed Scopus Google the acid our of the TagB reaction that glycerol phosphate and a were acid the of for the proposed reaction of teichoic acid biogenesis, we the of the TagF reaction with reaction in a on a of with a role for TagF as the poly(glycerol phosphate) polymerase (11Schertzer J.W. Brown E.D. J. Biol. Chem. 2003; 278: 18002-18007Abstract Full Text Full Text PDF PubMed Scopus (36) Google Scholar). Here we demonstrate of the TagB reaction with a of a the TagF and with the of a glycerol phosphate to the Nevertheless, we to the in the reaction we the that TagB a glycerol phosphate to the the data in this study are with the that TagB the transfer of glycerol phosphate from CDP-glycerol to an we the that the protein that TagB for in vitro were with the of TagB We were incorporation of labeled glycerol phosphate onto the membrane this It is the of to the of the membrane or to in The to the studies also that membrane from B. subtilis 168 and were functional in the TagB is not that the glycerol phosphate reaction is to on membrane-bound in the the of the the of of glycerol phosphate to the (13Lazarevic V. Abellan F.X. Moller S.B. Karamata D. Mauel C. Microbiology. 2002; 148: 815-824Crossref PubMed Scopus (69) Google Scholar). of this the of TagB from B. subtilis protein sequence with The of the that TagB for the enzymatic in this the accompanying J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar), we the of in TagB and TagF the of a teichoic acid biosynthesis in The enzymatic for the that the in TagF J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). our understanding of the reaction for TagB and TagF are that it is steps in these are to either that TagF is a polymerase and TagB is a it is that the steps be Nevertheless, the in and have the role in reaction as a be in our in vitro in the case of of in this to the J.W. A.P. Brown E.D. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). it is not of TagB is for of this Nevertheless, the TagB and TagF a of in to the evidence provided in this strongly suggests that TagB is the CDP-glycerol:N-acetyl-β-d-mannosaminyl-1,4-N-acetyl-d-glucosaminyldiphosphoundecaprenyl or these studies for the the of the proteins as a involved in We the of the provided and provided and of the for and

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